ID Q9DTF0_9HEPC Unreviewed; 3010 AA. AC Q9DTF0; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 25-MAY-2022, entry version 149. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Hepacivirus C. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Hepacivirus. OX NCBI_TaxID=11103 {ECO:0000313|EMBL:BAB18800.1, ECO:0000313|Proteomes:UP000117176}; RN [1] {ECO:0000313|EMBL:BAB18800.1, ECO:0000313|Proteomes:UP000117176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HCVT050 {ECO:0000313|EMBL:BAB18800.1}; RX PubMed=11348851; DOI=10.1016/S1386-6346(00)00141-8; RA Takahashi K., Iwata K., Matsumoto M., Matsumoto H., Nakao K., Hatahara T., RA Ohta Y., Kanai K., Maruo H., Baba K., Hijikata M., Mishiro S.; RT "Hepatitis C virus (HCV) genotype 1b sequences from fifteen patients with RT hepatocellular carcinoma: the 'progression score' revisited."; RL Hepatol. Res. 20:161-171(2001). CC -!- FUNCTION: RNA-dependent RNA polymerase that performs primer-template CC recognition and RNA synthesis during viral replication. CC {ECO:0000256|ARBA:ARBA00023584}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC Evidence={ECO:0000256|ARBA:ARBA00001556}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of four peptide bonds in the viral precursor CC polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr CC in P1 and Ser or Ala in P1'.; EC=3.4.21.98; CC Evidence={ECO:0000256|ARBA:ARBA00001117}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CC Evidence={ECO:0000256|ARBA:ARBA00001491}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum CC membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004406}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004389}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004115}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004165}. Host cytoplasm, host perinuclear CC region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic reticulum CC membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004291}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004291}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004517}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004517}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004482}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004482}. Host lipid droplet CC {ECO:0000256|ARBA:ARBA00004338}. Host mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004458}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004458}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Lipid droplet CC {ECO:0000256|ARBA:ARBA00004502}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Membrane CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004167}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004583}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004563}. CC -!- SIMILARITY: Belongs to the hepacivirus polyprotein family. CC {ECO:0000256|ARBA:ARBA00008286}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB049087; BAB18800.1; -; Genomic_RNA. DR PIR; A61196; A61196. DR PIR; PQ0246; PQ0246. DR PIR; PQ0251; PQ0251. DR PIR; PQ0252; PQ0252. DR PIR; PQ0254; PQ0254. DR PIR; PS0329; PS0329. DR MEROPS; S29.001; -. DR euHCVdb; AB049087; -. DR Proteomes; UP000117176; Genome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW. DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW. DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW. DR GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 1.20.1280.150; -; 1. DR Gene3D; 2.20.25.210; -; 1. DR Gene3D; 2.20.25.220; -; 1. DR Gene3D; 2.30.30.710; -; 1. DR Gene3D; 2.40.10.10; -; 1. DR Gene3D; 3.30.70.270; -; 2. DR Gene3D; 3.40.50.300; -; 2. DR Gene3D; 4.10.710.10; -; 1. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR002521; HCV_Core_C. DR InterPro; IPR044896; HCV_core_chain_A. DR InterPro; IPR002522; HCV_core_N. DR InterPro; IPR002519; HCV_Env. DR InterPro; IPR002531; HCV_NS1. DR InterPro; IPR002518; HCV_NS2. DR InterPro; IPR042205; HCV_NS2_C. DR InterPro; IPR042209; HCV_NS2_N. DR InterPro; IPR000745; HCV_NS4a. DR InterPro; IPR001490; HCV_NS4b. DR InterPro; IPR002868; HCV_NS5a. DR InterPro; IPR013192; HCV_NS5A_1a. DR InterPro; IPR013193; HCV_NS5a_1B_dom. DR InterPro; IPR038568; HCV_NS5A_1B_sf. DR InterPro; IPR024350; HCV_NS5a_C. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR004109; NS3_Peptidase_S29. DR InterPro; IPR038170; NS5A_1a_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002166; RNA_pol_HCV. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF01543; HCV_capsid; 1. DR Pfam; PF01542; HCV_core; 1. DR Pfam; PF01539; HCV_env; 1. DR Pfam; PF01560; HCV_NS1; 1. DR Pfam; PF01538; HCV_NS2; 1. DR Pfam; PF01006; HCV_NS4a; 1. DR Pfam; PF01001; HCV_NS4b; 1. DR Pfam; PF01506; HCV_NS5a; 1. DR Pfam; PF08300; HCV_NS5a_1a; 1. DR Pfam; PF08301; HCV_NS5a_1b; 1. DR Pfam; PF12941; HCV_NS5a_C; 1. DR Pfam; PF02907; Peptidase_S29; 1. DR Pfam; PF00998; RdRP_3; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF56672; SSF56672; 1. DR PROSITE; PS51693; HCV_NS2_PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51822; HV_PV_NS3_PRO; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050}; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570}; Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|ARBA:ARBA00022506}; KW G1/S host cell cycle checkpoint dysregulation by virus KW {ECO:0000256|ARBA:ARBA00023309}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184}; KW Host lipid droplet {ECO:0000256|ARBA:ARBA00023190}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host mitochondrion {ECO:0000256|ARBA:ARBA00023147}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host MAVS by virus {ECO:0000256|ARBA:ARBA00022986}; KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482}; KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961}; KW Inhibition of host TRAFs by virus {ECO:0000256|ARBA:ARBA00022647}; KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Modulation of host cell cycle by virus {ECO:0000256|ARBA:ARBA00022504}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039}; KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT TRANSMEM 264..287 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 368..388 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 718..741 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 753..778 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 785..802 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 891..913 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1660..1688 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1825..1845 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1851..1870 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1882..1902 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2990..3007 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 903..1026 FT /note="Peptidase C18" FT /evidence="ECO:0000259|PROSITE:PS51693" FT DOMAIN 1027..1208 FT /note="Peptidase S29" FT /evidence="ECO:0000259|PROSITE:PS51822" FT DOMAIN 1217..1369 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1361..1538 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2633..2751 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2351..2407 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 2487..2507 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 47..68 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2351..2385 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 3010 AA; 327156 MW; 7A9C7B1273266FF3 CRC64; MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG RRQPIPKARQ PEGRAWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GGPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTIPAS AYEVRNVSGV YHVTNDCSNS SIVYEAADMI MHTPGCVPCV RENDCSRCWV ALTPTLAARN SSIPTTTIRR HVDLLVGAAA FCSAMYVGDL CGSIFLVSQL FTFSPRRYWT VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQSVVDMVAG AHWGVLAGLA YYSMVGNWAK VLIVMLLFAG VDGVTHMTGG QVSHNTRSFM SLFTCGPSQK IQLINTNGSW HINRTALNCN DSLQTGFLAA LFYAHNLNSS GCPERMASCR SIDKFAQGWG PITHVVPDTW DQRPYCWHYA PKPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGVPTYTWG ENETDVLFLN NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNNTLI CPTDCFRKHP EATYTKCGSG PWLTPRCMVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL NAACNWTRGE RCDLEDRDRS ELSPLLLSTT EWQVLPCSFT PLPALSTGLI HLHQNIVDVQ YLYGIGSAVV SVVIKWEYVL LLFLLLADAR VCSCLWMMLL IAQAEAALEN LVVLNAASVA GAHGTLSFLV FFCAAWYIKG KLVPGAAYAL YGVWPLLLLL LALPHRAYAM DPEMAASCGG AVFVGLALLT LSPHYKAFLA RLIWWLQYFI TRAEAHLQVW IPPLNVRGGR DAIILLACAV HPELIFDITK ILLAILGPLM VLQAGLTRVP YFVRAQGLIR VCMLVRKVAG GHYFQMALMK LAALTGTYVY DHLTPLRDWA HVGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIISGL PVSARRGREI LLGPADSFRE QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT VYHGAGSKTL AGPKGPITQM YTNVDQDLVG WQAPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG SLLSPRPVSY LKGSSGGPLL CPSGHAVGIF RAAVCTRGVA KAVDFIPVES METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA TLSFGAYMSK AHGVDPNIRT GVRTITTGAP ITYSTYGKFL ADGGCSGGAY DIIICDECHS TDSTSILGIG TVLDQAETAG ARLVLLATAT PPGSVTVPHP NIEEVALSNT GEIPFYGKAI PIETIKGGRH LIFCHSKKKC DELAAKLSAL GVNAVAYYRG LDVSVIPTSG NVVVVATDAL MTGYTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRAGIYR FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKFIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV VIVGRIILSG KPAVIPDREV LYREFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP LTTQHTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA GALVAFKVMS GEMPSAEDMV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FKTWLQSKLL PRLPGVPFFS CQRGYKGVWL GDGVMQTTCP CGAQISGHVK NGSMKIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGEFH YVTGMTTDNV KCPCQVPSPE FFTEVDGVRL HRYAPACKPL LRDEVTFQVG LNQYPVGSQL PCEPEPDVAV LTSMLTDPSH ITAETARRRL ARGSPPSLAS SSASQLSAPS LKATCTTCHD SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFDPLR AEEDEREVSV AAEILRKTRK FPPAIPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPPTK APPIPPPRRK RTVILTESTV SSALAELATK TFGSSGSSAV DSGTATAPPD QPSDDGDTGS DVGSYSSMPP LEGEPGDPDL SDGSWSTVSE EAGEDVVCCS MSYTWTGALI TPCGAEETKL PINALSNSLL RHHNMVYATT SRSASQRQRK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK LLSVEEACKL TPPHSARSKF GYGAKDVRNL SSKAVNHIRS VWKDLLEDTE TPINTTIMAK SEVFCVQPEK GGRKPARLIV FPDLGVRVCE KMALYDVVST LPQAVMGSSY GFQYSPGQRV EFLVNAWKSK KSPMGFAYDT RCFDSTVTES DIRVEESIYQ CCDLAPEARQ VIRSLTERLY IGGPLTNSKG QNCGYRRCRA SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVCGDDLV VICESAGTQE DAANLRVFTE AMTRYSAPPG DPPRPEYDLE LITSCSSNVS VAHDAAGKRV YYLTRDPITP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAV YSIEPLDLPQ IIQRLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRVWR HRARSVRAKL LSQGGRAATC GKYLFNWAVR TKLKLTPIPA ASQLDLSGWF VAGYSGGDIY HSLSRARPRW FMWCLLLLSV GVGIYLLPNR //